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Neurodegenerative diseases and oxidative stress

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Reactive Oxygen Species (ROS)-Based Nanomedicine

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The neurobiology of zinc in health and disease

Frederickson, C. J., Koh, J., & Bush, A. I. (2005) · Nature reviews. Neuroscience · doi:10.1038/nrn1671 · Cited by 1,841

Copper Homeostasis and Neurodegenerative Disorders (Alzheimer's, Prion, and Parkinson's Diseases and Amyotrophic Lateral Sclerosis)

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Effects of antioxidant enzymes in the molecular control of reactive oxygen species toxicology

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Role of Free Radicals in the Neurodegenerative Diseases: Therapeutic Implications for Antioxidant Treatment

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Treatment with a Copper-Zinc Chelator Markedly and Rapidly Inhibits β-Amyloid Accumulation in Alzheimer's Disease Transgenic Mice

Cherny, R. A., Atwood, C. S., Xilinas, M. E., Gray, D. N., Jones, W. D., McLean, C. A., Barnham, K. J., Volitakis, I., Fraser, F. W., Kim, Y.-S., et al. (2001) · Neuron · doi:10.1016/s0896-6273(01)00317-8 · Cited by 1,447

The metallobiology of Alzheimer's disease

Bush, A. I. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(03)00067-5 · Cited by 1,315

Role of Catalase in Oxidative Stress- and Age-Associated Degenerative Diseases

Nandi, A., Yan, L.-J., Jana, C. K., & Das, N. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9613090 · Cited by 1,185

Metals, oxidative stress and neurodegenerative disorders

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Selective neuronal vulnerability to oxidative stress in the brain

Wang, X. (2010) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2010.00012 · Cited by 1,043

Antioxidant Activity/Capacity Measurement. 1. Classification, Physicochemical Principles, Mechanisms, and Electron Transfer (ET)-Based Assays

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Early-onset Amyloid Deposition and Cognitive Deficits in Transgenic Mice Expressing a Double Mutant Form of Amyloid Precursor Protein 695

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The Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization

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Oxidative Stress and Neurotoxicity

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Oxidative Stress and the Pathogenesis of Alzheimer's Disease

Zhao, Y., & Zhao, B. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/316523 · Cited by 855

Oxidative stress in Alzheimer’s disease

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Oxidative stress and nitration in neurodegeneration: Cause, effect, or association?

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Review: Alzheimer's Amyloid β-Peptide-Associated Free Radical Oxidative Stress and Neurotoxicity

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Metals and neuroscience

Bush, A. (2000) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(99)00073-3 · Cited by 731

Rapid Restoration of Cognition in Alzheimer's Transgenic Mice with 8-Hydroxy Quinoline Analogs Is Associated with Decreased Interstitial Aβ

Adlard, P. A., Cherny, R. A., Finkelstein, D. I., Gautier, E., Robb, E., Cortes, M., Volitakis, I., Liu, X., Smith, J. P., Perez, K., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.06.018 · Cited by 672

Alzheimer's Disease Amyloid-β Binds Copper and Zinc to Generate an Allosterically Ordered Membrane-penetrating Structure Containing Superoxide Dismutase-like Subunits

Curtain, C. C., Ali, F. E. A., Volitakis, I., Cherny, R. A., Norton, R. S., Beyreuther, K. T., Barrow, C. J., Masters, C. L., Bush, A. I., & Barnham, K. J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100175200 · Cited by 658

Characterization of Copper Interactions with Alzheimer Amyloid β Peptides: Identification of an Attomolar‐Affinity Copper Binding Site on Amyloid β1‐42

Atwood, C. S., Scarpa, R. C., Huang, X., Moir, R. D., Jones, W. D., Fairlie, D. P., Tanzi, R. E., & Bush, A. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0751219.x · Cited by 641

Alzheimer's Disease: From Pathology to Therapeutic Approaches

Jakob‐Roetne, R., & Jacobsen, H. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200802808 · Cited by 626

Genetic or Pharmacological Iron Chelation Prevents MPTP-Induced Neurotoxicity In Vivo

Kaur, D., Yantiri, F., Rajagopalan, S., Kumar, J., Mo, J. Q., Boonplueang, R., Viswanath, V., Jacobs, R., Yang, L., Beal, M. F., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00126-0 · Cited by 620

The redox chemistry of the Alzheimer's disease amyloid β peptide

Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608

Iron neurochemistry in Alzheimer's disease and Parkinson's disease: targets for therapeutics

Belaidi, A. A., & Bush, A. I. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13425 · Cited by 594

Metalloenzyme-like Activity of Alzheimer's Disease β-Amyloid

Opazo, C., Huang, X., Cherny, R. A., Moir, R. D., Roher, A. E., White, A. R., Cappai, R., Masters, C. L., Tanzi, R. E., Inestrosa, N. C., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206428200 · Cited by 587

Therapeutics for Alzheimer's Disease Based on the Metal Hypothesis

Bush, A. I., & Tanzi, R. E. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.001 · Cited by 582

Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases

Kell, D. B. (2009) · BMC Medical Genomics · doi:10.1186/1755-8794-2-2 · Cited by 554

Bioinorganic chemistry of copper and zinc ions coordinated to amyloid-β peptide

Faller, P., & Hureau, C. (2009) · Dalton Trans. · doi:10.1039/b813398k · Cited by 530

Copper in disorders with neurological symptoms: Alzheimer’s, Menkes, and Wilson diseases

Strausak, D., Mercer, J. F. B., Dieter, H. H., Stremmel, W., & Multhaup, G. (2001) · Brain Research Bulletin · doi:10.1016/s0361-9230(01)00454-3 · Cited by 508

Copper in the brain and Alzheimer’s disease

Hung, Y. H., Bush, A. I., & Cherny, R. A. (2009) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-009-0600-y · Cited by 503

Biological metals and metal-targeting compounds in major neurodegenerative diseases

Barnham, K. J., & Bush, A. I. (2014) · Chem. Soc. Rev. · doi:10.1039/c4cs00138a · Cited by 497

Dietary supplementation with resveratrol reduces plaque pathology in a transgenic model of Alzheimer's disease

Karuppagounder, S. S., Pinto, J. T., Xu, H., Chen, H., Beal, M. F., & Gibson, G. E. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.10.008 · Cited by 495

Striking while the iron is hot: Iron metabolism and ferroptosis in neurodegeneration

Masaldan, S., Bush, A. I., Devos, D., Rolland, A., & Moreau, C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.09.033 · Cited by 494

Copper Binding to the Amyloid-β (Aβ) Peptide Associated with Alzheimer's Disease

Syme, C. D., Nadal, R. C., Rigby, S. E. J., & Viles, J. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313572200 · Cited by 459

Metal dyshomeostasis and oxidative stress in Alzheimer’s disease

Greenough, M. A., Camakaris, J., & Bush, A. I. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.08.014 · Cited by 447

Copper, zinc and iron in neurodegenerative diseases (Alzheimer's, Parkinson's and prion diseases)

Kozłowski, H., Łuczkowski, M., Remelli, M., & Valensin, D. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.013 · Cited by 446

Redox‐Active Metals, Oxidative Stress, and Alzheimer's Disease Pathology

HUANG, X., MOIR, R. D., TANZI, R. E., BUSH, A. I., & ROGERS, J. T. (2004) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1306.012 · Cited by 425

The chemistry of Alzheimer’s disease

Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417

Structural characterization of copper(II) binding to α-synuclein: Insights into the bioinorganic chemistry of Parkinson's disease

Rasia, R. M., Bertoncini, C. W., Marsh, D., Hoyer, W., Cherny, D., Zweckstetter, M., Griesinger, C., Jovin, T. M., & Fernández, C. O. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407881102 · Cited by 412

Targeted nanoparticles for drug delivery through the blood–brain barrier for Alzheimer's disease

Roney, C. A., Kulkarni, P. V., Arora, V., Antich, P. P., Bonte, F. J., Wu, A., Mallikarjuana, N. N., Manohar, S. K., Liang, H., Kulkarni, A. R., et al. (2005) · Journal of Controlled Release · doi:10.1016/j.jconrel.2005.07.024 · Cited by 411

Oxidative Stress, Amyloid-β Peptide, and Altered Key Molecular Pathways in the Pathogenesis and Progression of Alzheimer’s Disease

Butterfield, D. A., & Boyd-Kimball, D. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170543 · Cited by 403

Evidence that the β-Amyloid Plaques of Alzheimer's Disease Represent the Redox-silencing and Entombment of Aβ by Zinc

Cuajungco, M. P., Goldstein, L. E., Nunomura, A., Smith, M. A., Lim, J. T., Atwood, C., Huang, X., Farrag, Y. W., Perry, G. L., & Bush, A. I. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000165200 · Cited by 392

Oxidative stress signalling in Alzheimer's disease

Zhu, X., Raina, A. K., Lee, H., Casadesús, G., Smith, M. A., & Perry, G. L. (2004) · Brain Research · doi:10.1016/j.brainres.2004.01.012 · Cited by 396

Clusterin in Alzheimer’s Disease: Mechanisms, Genetics, and Lessons From Other Pathologies

Foster, E. M., Dangla-Valls, A., Lovestone, S., Ribe, E. M., & Buckley, N. J. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00164 · Cited by 381

Redox-active iron mediates amyloid-β toxicity

Rottkamp, C. A., Raina, A. K., Zhu, X., Gaier, E., Bush, A. I., Atwood, C., Chevion, M., Perry, G. L., & Smith, M. A. (2001) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(00)00494-9 · Cited by 379

Methionine oxidation by reactive oxygen species: reaction mechanisms and relevance to Alzheimer's disease

Schöneich, C. (2004) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.09.009 · Cited by 372

The role of oxidative stress in the toxicity induced by amyloid β-peptide in Alzheimer’s disease

Miranda, S., Opazo, C., Larrondo, L. F., Muñoz, F. J., Ruiz, F., Leighton, F., & Inestrosa, N. C. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(00)00015-0 · Cited by 369

Synaptically released zinc: Physiological functions and pathological effects

Frederickson, C. J., & Bush, A. I. (2001) · BioMetals · doi:10.1023/a:1012934207456 · Cited by 360

Metallostasis in Alzheimer's disease

Ayton, S., Lei, P., & Bush, A. I. (2012) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2012.10.558 · Cited by 359

Metals and amyloid‐β in Alzheimer's disease

Maynard, C. J., Bush, A. I., Masters, C. L., Cappai, R., & Li, Q. (2005) · International Journal of Experimental Pathology · doi:10.1111/j.0959-9673.2005.00434.x · Cited by 356

Overexpression of Alzheimer's Disease Amyloid-β Opposes the Age-dependent Elevations of Brain Copper and Iron

Maynard, C. J., Cappai, R., Volitakis, I., Cherny, R. A., White, A. R., Beyreuther, K. T., Masters, C. L., Bush, A. I., & Li, Q. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m204379200 · Cited by 352

Biological inorganic and bioinorganic chemistry of neurodegeneration based on prion and Alzheimer diseases

Brown, D. R., & Kozłowski, H. (2004) · Dalton Transactions · doi:10.1039/b401985g · Cited by 343

Oxidative stress in Alzheimer's disease

Chauhan, V. P. S., & Chauhan, A. (2006) · Pathophysiology · doi:10.1016/j.pathophys.2006.05.004 · Cited by 349

Medicinal Inorganic Chemistry Approaches to Passivation and Removal of Aberrant Metal Ions in Disease

Scott, L. E., & Orvig, C. (2009) · Chemical Reviews · doi:10.1021/cr9000176 · Cited by 332

The essential elements of Alzheimer’s disease

Lei, P., Ayton, S., & Bush, A. I. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.rev120.008207 · Cited by 344

Copper-Dependent Inhibition of Human Cytochrome c Oxidase by a Dimeric Conformer of Amyloid-β1-42

Crouch, P. J., Blake, R., Duce, J. A., Ciccotosto, G. D., Li, Q.-X., Barnham, K. J., Curtain, C. C., Cherny, R. A., Cappai, R., Dyrks, T., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.4276-04.2005 · Cited by 327

Dietary Cu stabilizes brain superoxide dismutase 1 activity and reduces amyloid Aβ production in APP23 transgenic mice

Bayer, T. A., Schäfer, S., Simons, A., Kemmling, A., Kamer, T., Tepest, R., Eckert, A., Schüssel, K., Eikenberg, O., Sturchler, C., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2332818100 · Cited by 329

The Antioxidant Mechanisms Underlying the Aged Garlic Extract- and S-Allylcysteine-Induced Protection

Colín-González, A. L., Santana-Martínez, R. A., Silva‐Islas, C. A., Chánez‐Cárdenas, M. E., Santamarı́a, A., & Maldonado, P. D. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/907162 · Cited by 329

Metal complexing agents as therapies for Alzheimer’s disease

Bush, A. I. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00120-3 · Cited by 310

Dementia of Alzheimer’s disease and other neurodegenerative disorders—memantine, a new hope

Sonkusare, S. K., Kaul, C. L., & Ramarao, P. (2004) · Pharmacological Research · doi:10.1016/j.phrs.2004.05.005 · Cited by 313

Nanotechnology-based drug delivery systems for the treatment of Alzheimer’s disease

Fonseca‐Santos, B., Chorilli, M., & Gremião, M. P. D. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s87148 · Cited by 320

A Novel Function of Monomeric Amyloid β-Protein Serving as an Antioxidant Molecule against Metal-Induced Oxidative Damage

Zou, K., Gong, J.-S., Yanagisawa, K., & Michikawa, M. (2002) · The Journal of Neuroscience · doi:10.1523/jneurosci.22-12-04833.2002 · Cited by 305

Management of oxidative stress and other pathologies in Alzheimer’s disease

Simunkova, M., Alwasel, S. H., Alhazza, I. M., Jomova, K., Kollar, V., Rusko, M., & Valko, M. (2019) · Archives of Toxicology · doi:10.1007/s00204-019-02538-y · Cited by 303

Antioxidant neuroprotection in Alzheimer’s disease as preventive and therapeutic approach2 2This article is part of a series of reviews on “Causes and Consequences of Oxidative Stress in Alzheimer’s Disease.” The full list of papers may be found on the homepage of the journal.

Behl, C., & Moosmann, B. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00883-3 · Cited by 303

Amyloid-β: a chameleon walking in two worlds: a review of the trophic and toxic properties of amyloid-β

Atwood, C., Obrenovich, M. E., Liu, T., Chan, H., Perry, G. L., Smith, M. A., & Martins, R. N. (2003) · Brain Research Reviews · doi:10.1016/s0165-0173(03)00174-7 · Cited by 297

Copper and Oxidative Stress in the Pathogenesis of Alzheimer’s Disease

Eskici, G., & Axelsen, P. H. (2012) · Biochemistry · doi:10.1021/bi3006169 · Cited by 291

Aluminium in Alzheimer?s disease: are we still at a crossroad?

Gupta, V. B., Anitha, S., Hegde, M. L., Zecca, L., Garruto, R. M., Ravid, R., Shankar, S. K., Stein, R., Shanmugavelu, P., & Rao, K. S. J. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4317-3 · Cited by 294

Copper and Zinc Binding to Amyloid‐β: Coordination, Dynamics, Aggregation, Reactivity and Metal‐Ion Transfer

Faller, P. (2009) · ChemBioChem · doi:10.1002/cbic.200900321 · Cited by 285

Pyruvate Released by Astrocytes Protects Neurons from Copper-Catalyzed Cysteine Neurotoxicity

Wang, X. F., & Cynader, M. S. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-10-03322.2001 · Cited by 287

Biological metals and Alzheimer's disease: Implications for therapeutics and diagnostics

Duce, J. A., & Bush, A. I. (2010) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2010.04.003 · Cited by 288

Ribosomal RNA in Alzheimer Disease Is Oxidized by Bound Redox-active Iron

Honda, K., Smith, M. A., Zhu, X., Baus, D., Merrick, W. C., Tartakoff, A. M., Hattier, T., Harris, P. L., Siedlak, S. L., Fujioka, H., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500526200 · Cited by 280

Neuroprotective effects of apigenin against inflammation, neuronal excitability and apoptosis in an induced pluripotent stem cell model of Alzheimer’s disease

Balez, R., Steiner, N., Engel, M., Muñoz, S. S., Lum, J. S., Wu, Y., Wang, D., Vallotton, P., Sachdev, P. S., O’Connor, M. D., et al. (2016) · Scientific Reports · doi:10.1038/srep31450 · Cited by 280

Elevated cortical zinc in Alzheimer disease

Religa, D., Strozyk, D., Cherny, R. A., Volitakis, I., Haroutunian, V., Winblad, B. G., Näslund, J., & Bush, A. I. (2006) · Neurology · doi:10.1212/01.wnl.0000223644.08653.b5 · Cited by 273

Structure of the Alzheimer's Disease Amyloid Precursor Protein Copper Binding Domain

Barnham, K. J., McKinstry, W. J., Multhaup, G., Galatis, D., Morton, C. J., Curtain, C. C., Williamson, N. A., White, A. R., Hinds, M. G., Norton, R. S., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300629200 · Cited by 274

Redox Chemistry of Copper–Amyloid‐β: The Generation of Hydroxyl Radical in the Presence of Ascorbate is Linked to Redox‐Potentials and Aggregation State

Guilloreau, L., Combalbert, S., Sournia‐Saquet, A., Mazarguil, H., & Faller, P. (2007) · ChemBioChem · doi:10.1002/cbic.200700111 · Cited by 273

Homocysteine potentiates β‐amyloid neurotoxicity: role of oxidative stress

Ho, P. I., Collins, S. C., Dhitavat, S., Ortiz, D., Ashline, D. J., Rogers, E. J., & Shea, T. B. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00384.x · Cited by 271

Novel Tacrine−8-Hydroxyquinoline Hybrids as Multifunctional Agents for the Treatment of Alzheimer’s Disease, with Neuroprotective, Cholinergic, Antioxidant, and Copper-Complexing Properties

Fernández‐Bachiller, M. I., Pérez, C., González-Muñoz, G. C., Conde, S., López, M. G., Villarroya, M., Garcı́a, A. G., & Rodrı́guez-Franco, M. I. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100329q · Cited by 270

Dietary Copper and High Saturated and trans Fat Intakes Associated With Cognitive Decline

Morris, M. C., Evans, D. A., Tangney, C., Bienias, J. L., Schneider, J. A., Wilson, R. S., & Scherr, P. A. (2006) · Archives of Neurology · doi:10.1001/archneur.63.8.1085 · Cited by 270

The critical role of methionine 35 in Alzheimer's amyloid β-peptide (1–42)-induced oxidative stress and neurotoxicity

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